ID   METE_SULAC              Reviewed;         339 AA.
AC   Q4JAI4;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Methionine synthase {ECO:0000255|HAMAP-Rule:MF_00288};
DE            EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_00288};
DE   AltName: Full=Homocysteine methyltransferase {ECO:0000255|HAMAP-Rule:MF_00288};
GN   Name=metE {ECO:0000255|HAMAP-Rule:MF_00288}; OrderedLocusNames=Saci_0828;
OS   Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS   15157 / NCIMB 11770).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=330779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX   PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA   Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA   Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT   "The genome of Sulfolobus acidocaldarius, a model organism of the
RT   Crenarchaeota.";
RL   J. Bacteriol. 187:4992-4999(2005).
CC   -!- FUNCTION: Catalyzes the transfer of a methyl group to L-homocysteine
CC       resulting in methionine formation. The physiological methyl donor is
CC       unknown. {ECO:0000255|HAMAP-Rule:MF_00288}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00288};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00288};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC       pathway. {ECO:0000255|HAMAP-Rule:MF_00288}.
CC   -!- SIMILARITY: Belongs to the archaeal MetE family. {ECO:0000255|HAMAP-
CC       Rule:MF_00288, ECO:0000305}.
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DR   EMBL; CP000077; AAY80195.1; -; Genomic_DNA.
DR   RefSeq; WP_011277697.1; NC_007181.1.
DR   AlphaFoldDB; Q4JAI4; -.
DR   SMR; Q4JAI4; -.
DR   STRING; 330779.Saci_0828; -.
DR   PRIDE; Q4JAI4; -.
DR   EnsemblBacteria; AAY80195; AAY80195; Saci_0828.
DR   GeneID; 3472664; -.
DR   KEGG; sai:Saci_0828; -.
DR   PATRIC; fig|330779.12.peg.792; -.
DR   eggNOG; arCOG01876; Archaea.
DR   HOGENOM; CLU_040013_3_2_2; -.
DR   OMA; DPDCGMR; -.
DR   UniPathway; UPA00051; -.
DR   Proteomes; UP000001018; Chromosome.
DR   GO; GO:0003871; F:5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd03311; CIMS_C_terminal_like; 1.
DR   Gene3D; 3.20.20.210; -; 1.
DR   HAMAP; MF_00288; MetE; 1.
DR   InterPro; IPR002629; Met_Synth_C/arc.
DR   InterPro; IPR022921; MetE_arc.
DR   InterPro; IPR038071; UROD/MetE-like_sf.
DR   Pfam; PF01717; Meth_synt_2; 1.
DR   SUPFAM; SSF51726; SSF51726; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Metal-binding; Methionine biosynthesis;
KW   Methyltransferase; Reference proteome; Transferase; Zinc.
FT   CHAIN           1..339
FT                   /note="Methionine synthase"
FT                   /id="PRO_0000098691"
FT   BINDING         212
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00288"
FT   BINDING         214
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00288"
FT   BINDING         295
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00288"
SQ   SEQUENCE   339 AA;  39421 MW;  624BAFE6CA7F5CE4 CRC64;
     MSDEITILPT TVIGSYPRPK WLRETIRLHR AGKVNQEDLE EAFNDAVVTV VRDHQEAGID
     VPTDGEMRRD EMVEFFAERL SGFKFYGHVR VWGDHYYRKP SVTGKIKYNN PMLLDEVNFA
     KSVSYTQNLK VTITGPYTIS EWSYNEYYKT QRDMAFDLAK VINQEIKNLV DIGIKVIQVD
     EPAIHTRKED VEWAIDSINE SIKGVNVKVV LHVCYGEYSY LEPHLDKLKV DQINLALKNY
     NYTPVKLFKK WDREIGVGVI DVHNRKIESV EEVAEDLRKL LEYFKPEMVW VNPDCGLKLL
     PRKIALQKLI NMVKGTLIVR EELKKKGYTN TTLKPLINR